The linker histone in Saccharomyces cerevisiae interacts with actin-related protein 4 and both regulate chromatin structure and cellular morphology

Int J Biochem Cell Biol. 2015 Feb;59:182-92. doi: 10.1016/j.biocel.2014.12.006. Epub 2014 Dec 24.

Abstract

Chromatin structure promotes important epigenetic mechanisms that regulate cellular fate by organizing, preserving and controlling the way by which the genetic information works. Our understanding of chromatin and its functions is sparse and not yet well defined. The uncertainty comes from the complexity of chromatin and is induced by the existence of a large number of nuclear proteins that influence it. The intricate interaction among all these structural and functional nuclear proteins has been under extensive study in the recent years. Here, we show that Saccharomyces cerevisiae linker histone physically interacts with Arp4p (actin-related protein 4) which is a key subunit of three chromatin modifying complexes - INO80, SWR1 and NuA4. A single - point mutation in the actin - fold domain of Arp4p together with the knock-out of the gene for the linker histone in S. cerevisiae severely abrogates cellular and nuclear morphology and leads to complete disorganizing of the higher levels of chromatin organization.

Keywords: Actin-related protein 4 (Arp4p); Chromatin; Chromatin remodeling; Hho1p; higher-order chromatin structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Cell Shape
  • Chromatin / chemistry*
  • Chromatin / metabolism*
  • Comet Assay
  • Histones / metabolism*
  • Microscopy, Atomic Force
  • Models, Biological
  • Mutant Proteins / metabolism
  • Mutation
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Actins
  • Arp4 protein, S cerevisiae
  • Chromatin
  • HHO1 protein, S cerevisiae
  • Histones
  • Mutant Proteins
  • Nuclear Proteins
  • Saccharomyces cerevisiae Proteins